Gene Ontology annotation through association of InterPro records with GO terms
Annotation inferences using phylogenetic trees
Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
Automatic Gene Ontology annotation based on Rhea mapping
Electronic Gene Ontology annotations created by ARBA machine learning models
Combined Automated Annotation using Multiple IEA Methods
Characterization of MAD2B and other mitotic spindle checkpoint genes.
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Mapped the chromosomal locus of TTK (MPS1L1) alongside other spindle checkpoint genes and screened them for mutations in aneuploid colorectal tumours; the paper contains no localization or functional data on TTK.
"We determined the chromosomal localization of it and other spindle checkpoint genes, including MAD1L1, MAD2, BUB3, TTK (MPS1L1), and CDC20."
Expression of TTK, a novel human protein kinase, is associated with cell proliferation.
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Cloning of human TTK; the recombinant kinase domain generates phosphoserine and phosphothreonine strongly and phosphotyrosine weakly, and TTK mRNA is restricted to proliferating tissues, tumours and cell lines.
"Escherichia coli expressing the complete kinase domain of TTK contain markedly elevated levels of phosphoserine and phosphothreonine as well as slightly increased levels of phosphotyrosine"
Mps1 phosphorylates Borealin to control Aurora B activity and chromosome alignment.
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Human Mps1 directly phosphorylates Borealin/CDCA8 on residues required for Aurora B activity; cells without Mps1 kinase activity leave improper attachments uncorrected, and phosphomimetic Borealin restores alignment.
"Borealin/DasraB bearing phosphomimetic mutations restores Aurora B activity and alignment in Mps1-depleted cells"
Holding their own: the noncanonical roles of Smad proteins.
Spatiotemporal control of mitosis by the conserved spindle matrix protein Megator.
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In human cells TPR, MAD1, MAD2 and Mps1 co-immunoprecipitate from mitotic extracts and co-localize at the nuclear pore complex in interphase; Megator/TPR promotes timely recruitment of Mad2 and Mps1 to unattached kinetochores.
"Tpr, Mad1, Mad2, and Mps1 coimmunoprecipitate in mitotic enriched HeLa cell extracts prepared in the presence of nocodazole"
Defining the membrane proteome of NK cells.
MPS1/Mph1 phosphorylates the kinetochore protein KNL1/Spc7 to recruit SAC components.
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Mps1/Mph1 phosphorylates the MELT repeats of KNL1/Spc7 at unattached kinetochores to create the docking mark that recruits Bub1-Bub3 and initiates SAC signalling; the mechanism appears conserved in human cells.
"MPS1/Mph1 kinase locating at the unattached kinetochores initially creates a mark, which is crucial for SAC activation and chromosome bi-orientation. This mechanism seems to be conserved in human cells."
E-cadherin interactome complexity and robustness resolved by quantitative proteomics.
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Proximity-biotinylation proteomics of the E-cadherin environment, with GFP tagging used to assign subcellular localization to candidate proteins; source of the TTK cytoplasm IDA.
"by tagging identified proteins with GFP (green fluorescent protein), we determined the subcellular localization of 83 putative E-cadherin-proximal proteins"
CELL DIVISION CYCLE. Kinetochore attachment sensed by competitive Mps1 and microtubule binding to Ndc80C.
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Human Mps1 binds the NDC80 complex directly through two interactions that use the microtubule-binding surfaces of Ndc80C and are inhibited by microtubules; disrupting one interaction causes checkpoint defects.
"Competition between Mps1 and microtubules for Ndc80C binding thus constitutes a direct mechanism for the detection of unattached kinetochores."
Mps1 Regulates Kinetochore-Microtubule Attachment Stability via the Ska Complex to Ensure Error-Free Chromosome Segregation.
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Kinetochore-targeted Mps1 destabilises K-fibres independently of Aurora B; phosphoproteomics identifies Mps1-dependent Ser/Thr sites on KNL1, ROD, SKA3 and Mps1 itself; SKA3 Ser34 phosphorylation weakens end-coupled microtubule binding of the Ska complex, opposed by PP2A-B56.
"We also identify the Ska complex as a key effector of Mps1 at the kinetochore-microtubule interface, as mutations that mimic constitutive phosphorylation destabilized K fibers in vivo"
Mps1 regulates spindle morphology through MCRS1 to promote chromosome alignment.
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Mps1 binds and phosphorylates MCRS1 at Ser64/Ser65, enabling KIF2A localization to spindle microtubule minus ends and promoting chromosome alignment; phosphorylation is blocked by the Mps1 inhibitor reversine.
"Mps1 binds and phosphorylates MCRS1. This mechanism enables KIF2A localization to the minus end of spindle microtubules."
Yeast spindle pole body duplication gene MPS1 encodes an essential dual specificity protein kinase.
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Budding-yeast Mps1p is an essential kinase that autophosphorylates and phosphorylates serine, threonine and tyrosine in vitro; a kinase-dead allele behaves as a null, and the gene was identified through spindle pole body duplication defects.
"Phosphoamino acid analysis of substrates phosphorylated by Mps1p indicates that this kinase can phosphorylate serine, threonine and tyrosine residues, identifying Mps1p as a dual specificity protein kinase."
Deep research report on TTK